Glycoengineered keratinocyte library reveals essential functions of specific glycans for all stages of HSV-1 infection.

ABSTRACT: Viral and host glycans represent an understudied aspect of host-pathogen interactions, despite potential implications for treatment of viral infections. This is due to lack of easily accessible tools for analyzing glycan function in a meaningful context. Here we generate a glycoengineered keratinocyte library delineating human glycosylation pathways to uncover roles of specific glycans at different stages of herpes simplex virus type 1 (HSV-1) infectious cycle. We show the importance of cellular glycosaminoglycans and glycosphingolipids for HSV-1 attachment, N-glycans for entry and spread, and O-glycans for propagation. While altered virion surface structures have minimal effects on the early interactions with wild type cells, mutation of specific O-glycosylation sites affects glycoprotein

SUBMITTER: Bagdonaite I 

PROVIDER: S-EPMC10622544 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature